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Protein

POC1 centriolar protein homolog B

Gene

POC1B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays an important role in centriole assembly and/or stability and ciliogenesis (PubMed:20008567). Involved in early steps of centriole duplication, as well as in the later steps of centriole length control (PubMed:19109428). Acts in concert with POC1A to ensure centriole integrity and proper mitotic spindle formation. Required for primary cilia formation, ciliary length and also cell proliferation (PubMed:23015594). Required for retinal integrity (PubMed:25044745).4 Publications

GO - Biological processi

  • cell proliferation Source: UniProtKB
  • cilium assembly Source: UniProtKB
  • retina homeostasis Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation

Enzyme and pathway databases

SignaLinkiQ8TC44.

Names & Taxonomyi

Protein namesi
Recommended name:
POC1 centriolar protein homolog B
Alternative name(s):
Pix1
Proteome of centriole protein 1B
WD repeat-containing protein 51B
Gene namesi
Name:POC1B
Synonyms:WDR51B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:30836. POC1B.

Subcellular locationi

GO - Cellular componenti

  • centriole Source: UniProtKB
  • centrosome Source: UniProtKB
  • ciliary basal body Source: UniProtKB
  • spindle pole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Cone-rod dystrophy 20 (CORD20)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of cone-rod dystrophy, an inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa.
See also OMIM:615973
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671Missing in CORD20; disrupts interaction with FAM161A; localization of the mutant is cytosolic without enrichment at specific subcellular sites. 1 Publication
VAR_071916
Natural varianti106 – 1061R → P in CORD20; disrupts interaction with FAM161A; localization of the mutant is cytosolic without enrichment at specific subcellular sites. 3 Publications
Corresponds to variant rs76216585 [ dbSNP | Ensembl ].
VAR_071917

Keywords - Diseasei

Cone-rod dystrophy, Disease mutation

Organism-specific databases

MalaCardsiPOC1B.
MIMi615973. phenotype.
Orphaneti1872. Cone rod dystrophy.
PharmGKBiPA165513299.

Polymorphism and mutation databases

BioMutaiPOC1B.
DMDMi74762610.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 478478POC1 centriolar protein homolog BPRO_0000051410Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei321 – 3211PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated in mitotic cells that may be mediated by CDK1.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8TC44.
MaxQBiQ8TC44.
PaxDbiQ8TC44.
PeptideAtlasiQ8TC44.
PRIDEiQ8TC44.

PTM databases

iPTMnetiQ8TC44.
PhosphoSiteiQ8TC44.

Expressioni

Tissue specificityi

Expressed in the retina.1 Publication

Gene expression databases

BgeeiQ8TC44.
CleanExiHS_WDR51B.
ExpressionAtlasiQ8TC44. baseline and differential.
GenevisibleiQ8TC44. HS.

Organism-specific databases

HPAiHPA038841.

Interactioni

Subunit structurei

Interacts with POC1A (PubMed:23015594). Interacts with FAM161A (PubMed:25018096).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NUDCQ9Y2662EBI-1176274,EBI-357298

Protein-protein interaction databases

BioGridi129421. 47 interactions.
IntActiQ8TC44. 25 interactions.
STRINGi9606.ENSP00000323302.

Structurei

3D structure databases

ProteinModelPortaliQ8TC44.
SMRiQ8TC44. Positions 14-364.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati16 – 5540WD 1Add
BLAST
Repeati58 – 9942WD 2Add
BLAST
Repeati101 – 13939WD 3Add
BLAST
Repeati142 – 18140WD 4Add
BLAST
Repeati183 – 22341WD 5Add
BLAST
Repeati226 – 26540WD 6Add
BLAST
Repeati268 – 30740WD 7Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili431 – 47040Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi370 – 3756Poly-Thr

Sequence similaritiesi

Belongs to the WD repeat POC1 family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, WD repeat

Phylogenomic databases

eggNOGiENOG410IF90. Eukaryota.
ENOG410XR4H. LUCA.
GeneTreeiENSGT00810000125363.
HOGENOMiHOG000036743.
HOVERGENiHBG057502.
InParanoidiQ8TC44.
KOiK16482.
OMAiTFLMLWN.
PhylomeDBiQ8TC44.
TreeFamiTF324210.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 7 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 7 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8TC44-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASATEDPVL ERYFKGHKAA ITSLDLSPNG KQLATASWDT FLMLWNFKPH
60 70 80 90 100
ARAYRYVGHK DVVTSVQFSP HGNLLASASR DRTVRLWIPD KRGKFSEFKA
110 120 130 140 150
HTAPVRSVDF SADGQFLATA SEDKSIKVWS MYRQRFLYSL YRHTHWVRCA
160 170 180 190 200
KFSPDGRLIV SCSEDKTIKI WDTTNKQCVN NFSDSVGFAN FVDFNPSGTC
210 220 230 240 250
IASAGSDQTV KVWDVRVNKL LQHYQVHSGG VNCISFHPSG NYLITASSDG
260 270 280 290 300
TLKILDLLEG RLIYTLQGHT GPVFTVSFSK GGELFASGGA DTQVLLWRTN
310 320 330 340 350
FDELHCKGLT KRNLKRLHFD SPPHLLDIYP RTPHPHEEKV ETVEINPKLE
360 370 380 390 400
VIDLQISTPP VMDILSFDST TTTETSGRTL PDKGEEACGY FLNPSLMSPE
410 420 430 440 450
CLPTTTKKKT EDMSDLPCES QRSIPLAVTD ALEHIMEQLN VLTQTVSILE
460 470
QRLTLTEDKL KDCLENQQKL FSAVQQKS
Length:478
Mass (Da):53,668
Last modified:June 1, 2002 - v1
Checksum:i1D93DBBE05A603E8
GO
Isoform 2 (identifier: Q8TC44-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-42: Missing.

Note: Gene prediction based on EST data.
Show »
Length:436
Mass (Da):49,104
Checksum:i0570AE7A1F29DAD6
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671Missing in CORD20; disrupts interaction with FAM161A; localization of the mutant is cytosolic without enrichment at specific subcellular sites. 1 Publication
VAR_071916
Natural varianti106 – 1061R → P in CORD20; disrupts interaction with FAM161A; localization of the mutant is cytosolic without enrichment at specific subcellular sites. 3 Publications
Corresponds to variant rs76216585 [ dbSNP | Ensembl ].
VAR_071917

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4242Missing in isoform 2. CuratedVSP_047066Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK074772 mRNA. Translation: BAC11198.1.
AC010201 Genomic DNA. No translation available.
AC025034 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97425.1.
BC026080 mRNA. Translation: AAH26080.1.
CCDSiCCDS31869.1. [Q8TC44-1]
CCDS55859.1. [Q8TC44-2]
RefSeqiNP_001186706.1. NM_001199777.1. [Q8TC44-2]
NP_758440.1. NM_172240.2. [Q8TC44-1]
UniGeneiHs.25130.
Hs.604487.

Genome annotation databases

EnsembliENST00000313546; ENSP00000323302; ENSG00000139323. [Q8TC44-1]
ENST00000549035; ENSP00000447916; ENSG00000139323. [Q8TC44-2]
GeneIDi282809.
KEGGihsa:282809.
UCSCiuc001tba.4. human. [Q8TC44-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK074772 mRNA. Translation: BAC11198.1.
AC010201 Genomic DNA. No translation available.
AC025034 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97425.1.
BC026080 mRNA. Translation: AAH26080.1.
CCDSiCCDS31869.1. [Q8TC44-1]
CCDS55859.1. [Q8TC44-2]
RefSeqiNP_001186706.1. NM_001199777.1. [Q8TC44-2]
NP_758440.1. NM_172240.2. [Q8TC44-1]
UniGeneiHs.25130.
Hs.604487.

3D structure databases

ProteinModelPortaliQ8TC44.
SMRiQ8TC44. Positions 14-364.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi129421. 47 interactions.
IntActiQ8TC44. 25 interactions.
STRINGi9606.ENSP00000323302.

PTM databases

iPTMnetiQ8TC44.
PhosphoSiteiQ8TC44.

Polymorphism and mutation databases

BioMutaiPOC1B.
DMDMi74762610.

Proteomic databases

EPDiQ8TC44.
MaxQBiQ8TC44.
PaxDbiQ8TC44.
PeptideAtlasiQ8TC44.
PRIDEiQ8TC44.

Protocols and materials databases

DNASUi282809.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000313546; ENSP00000323302; ENSG00000139323. [Q8TC44-1]
ENST00000549035; ENSP00000447916; ENSG00000139323. [Q8TC44-2]
GeneIDi282809.
KEGGihsa:282809.
UCSCiuc001tba.4. human. [Q8TC44-1]

Organism-specific databases

CTDi282809.
GeneCardsiPOC1B.
HGNCiHGNC:30836. POC1B.
HPAiHPA038841.
MalaCardsiPOC1B.
MIMi614784. gene.
615973. phenotype.
neXtProtiNX_Q8TC44.
Orphaneti1872. Cone rod dystrophy.
PharmGKBiPA165513299.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IF90. Eukaryota.
ENOG410XR4H. LUCA.
GeneTreeiENSGT00810000125363.
HOGENOMiHOG000036743.
HOVERGENiHBG057502.
InParanoidiQ8TC44.
KOiK16482.
OMAiTFLMLWN.
PhylomeDBiQ8TC44.
TreeFamiTF324210.

Enzyme and pathway databases

SignaLinkiQ8TC44.

Miscellaneous databases

ChiTaRSiPOC1B. human.
GenomeRNAii282809.
PROiQ8TC44.
SOURCEiSearch...

Gene expression databases

BgeeiQ8TC44.
CleanExiHS_WDR51B.
ExpressionAtlasiQ8TC44. baseline and differential.
GenevisibleiQ8TC44. HS.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 7 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 7 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  2. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Testis.
  5. "Pix1 and Pix2 are novel WD40 microtubule-associated proteins that colocalize with mitochondria in Xenopus germ plasm and centrosomes in human cells."
    Hames R.S., Hames R., Prosser S.L., Euteneuer U., Lopes C.A., Moore W., Woodland H.R., Fry A.M.
    Exp. Cell Res. 314:574-589(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Basal body stability and ciliogenesis requires the conserved component Poc1."
    Pearson C.G., Osborn D.P., Giddings T.H. Jr., Beales P.L., Winey M.
    J. Cell Biol. 187:905-920(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "Molecular architecture of the centriole proteome: the conserved WD40 domain protein POC1 is required for centriole duplication and length control."
    Keller L.C., Geimer S., Romijn E., Yates J. III, Zamora I., Marshall W.F.
    Mol. Biol. Cell 20:1150-1166(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "Poc1A and Poc1B act together in human cells to ensure centriole integrity."
    Venoux M., Tait X., Hames R.S., Straatman K.R., Woodland H.R., Fry A.M.
    J. Cell Sci. 126:163-175(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH POC1A, PHOSPHORYLATION.
  10. Cited for: INTERACTION WITH FAM161A, INVOLVEMENT IN CORD20, VARIANTS CORD20 GLN-67 DEL AND PRO-106, CHARACTERIZATION OF VARIANTS CORD20 GLN-67 DEL AND PRO-106.
  11. Cited for: FUNCTION, TISSUE SPECIFICITY, VARIANT CORD20 PRO-106.
  12. "Novel recessive cone-rod dystrophy caused by POC1B mutation."
    Durlu Y.K., Koeroglu C., Tolun A.
    JAMA Ophthalmol. 132:1185-1191(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CORD20 PRO-106.

Entry informationi

Entry nameiPOC1B_HUMAN
AccessioniPrimary (citable) accession number: Q8TC44
Secondary accession number(s): G3V1X0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: June 1, 2002
Last modified: July 6, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.